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Conserved domains on  [gi|19076063|ref|NP_588563|]
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ankyrin repeat-containing protein [Schizosaccharomyces pombe]

Protein Classification

ankyrin repeat domain-containing protein( domain architecture ID 11429852)

ankyrin repeat domain-containing protein; ANK proteins mediate specific protein-protein interactions without necessarily recognizing specific primary sequences which allows for one ankyrin repeat domain to recognize and bind to a variety of intracellular substrates and may be involved in a wide array of functions

Gene Ontology:  GO:0005515
PubMed:  17176038
SCOP:  4000366

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
10-170 8.37e-17

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 76.53  E-value: 8.37e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076063  10 IAASDGKTDVVLKHLDSGISPNAADENGYTPIHAAVSYGHSDLLKILVERGGDINIRDQDGETPLFVC---EKLEIAHDL 86
Cdd:COG0666 126 LAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAaenGHLEIVKLL 205

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076063  87 INqYNADTTVKNNDGLIAAQVIEANGEFPELAKYLYSFTDLEPKDVNTLPNDTKIEYAKLMTEQEMDEEAGQPLLDQKAK 166
Cdd:COG0666 206 LE-AGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLD 284


                ....
gi 19076063 167 AEID 170
Cdd:COG0666 285 LLTL 288
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
10-170 8.37e-17

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 76.53  E-value: 8.37e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076063  10 IAASDGKTDVVLKHLDSGISPNAADENGYTPIHAAVSYGHSDLLKILVERGGDINIRDQDGETPLFVC---EKLEIAHDL 86
Cdd:COG0666 126 LAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAaenGHLEIVKLL 205

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076063  87 INqYNADTTVKNNDGLIAAQVIEANGEFPELAKYLYSFTDLEPKDVNTLPNDTKIEYAKLMTEQEMDEEAGQPLLDQKAK 166
Cdd:COG0666 206 LE-AGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLD 284


                ....
gi 19076063 167 AEID 170
Cdd:COG0666 285 LLTL 288
Ank_2 pfam12796
Ankyrin repeats (3 copies);
8-98 6.71e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 62.06  E-value: 6.71e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076063     8 IWIAASDGKTDVVLKHLDSGISPNAADENGYTPIHAAVSYGHSDLLKILVERgGDINIRDqDGETPLFVCEK---LEIAH 84
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARsghLEIVK 78

                          90
                  ....*....|....
gi 19076063    85 DLInQYNADTTVKN 98
Cdd:pfam12796  79 LLL-EKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 24-77 8.66e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 54.29  E-value: 8.66e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 19076063   24 LDSGISPNAADENGYTPIHAAVSYGHSDLLKILVERGGDINIRDQDGETPLFVC 77
Cdd:PHA03100 179 LSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIA 232
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 36-65 1.35e-06

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 43.35  E-value: 1.35e-06
                           10        20        30
                   ....*....|....*....|....*....|
gi 19076063     36 NGYTPIHAAVSYGHSDLLKILVERGGDINI 65
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 44-102 1.92e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 38.46  E-value: 1.92e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19076063  44 AVSYGHSDLLKILVERGGDINIRDQDGETPL----------FVCEkleiAHDLINQYNAD------TTVKNNDGL 102
Cdd:cd22192 143 AACVGNEEIVRLLIEHGADIRAQDSLGNTVLhilvlqpnktFACQ----MYDLILSYDKEddlqplDLVPNNQGL 213
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
10-170 8.37e-17

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 76.53  E-value: 8.37e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076063  10 IAASDGKTDVVLKHLDSGISPNAADENGYTPIHAAVSYGHSDLLKILVERGGDINIRDQDGETPLFVC---EKLEIAHDL 86
Cdd:COG0666 126 LAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAaenGHLEIVKLL 205

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076063  87 INqYNADTTVKNNDGLIAAQVIEANGEFPELAKYLYSFTDLEPKDVNTLPNDTKIEYAKLMTEQEMDEEAGQPLLDQKAK 166
Cdd:COG0666 206 LE-AGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLD 284


                ....
gi 19076063 167 AEID 170
Cdd:COG0666 285 LLTL 288
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
5-121 9.17e-16

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 73.83  E-value: 9.17e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076063   5 TPNIWIAASDGKTDVVLKHLDSGISPNAADENGYTPIHAAVSYGHSDLLKILVERGGDINIRDQDGETPLFV---CEKLE 81
Cdd:COG0666  88 NTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLaaaNGNLE 167

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 19076063  82 IAHDLInQYNADTTVKNNDG---LIAAqvieANGEFPELAKYL 121
Cdd:COG0666 168 IVKLLL-EAGADVNARDNDGetpLHLA----AENGHLEIVKLL 205
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
8-138 5.05e-14

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 68.83  E-value: 5.05e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076063   8 IWIAASDGKTDVVLKHLDSGISPNAADENGYTPIHAAVSYGHSDLLKILVERGGDINIRDQDGETPLF--VCEKLEIAHD 85
Cdd:COG0666 157 LHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDlaAENGNLEIVK 236

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 19076063  86 LINQYNADTTVKNNDGLIAAQVIEANGEFPELAKYLYSFTDLEPKDVNTLPND 138
Cdd:COG0666 237 LLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
Ank_2 pfam12796
Ankyrin repeats (3 copies);
8-98 6.71e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 62.06  E-value: 6.71e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076063     8 IWIAASDGKTDVVLKHLDSGISPNAADENGYTPIHAAVSYGHSDLLKILVERgGDINIRDqDGETPLFVCEK---LEIAH 84
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARsghLEIVK 78

                          90
                  ....*....|....
gi 19076063    85 DLInQYNADTTVKN 98
Cdd:pfam12796  79 LLL-EKGADINVKD 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
4-121 2.90e-11

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 61.12  E-value: 2.90e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076063   4 TTPNIWIAASDGKTDVVLKHLDSGISPNAADENGYTPIHAAVSYGHSDLLKILVERGGDINIRDQDGETPLFVC---EKL 80
Cdd:COG0666  54 GALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAaynGNL 133

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 19076063  81 EIAHDLInQYNADTTVKNNDG---LIAAqvieANGEFPELAKYL 121
Cdd:COG0666 134 EIVKLLL-EAGADVNAQDNDGntpLHLA----AANGNLEIVKLL 172
Ank_5 pfam13857
Ankyrin repeats (many copies);
28-74 4.99e-10

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 53.12  E-value: 4.99e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 19076063    28 ISPNAADENGYTPIHAAVSYGHSDLLKILVERGGDINIRDQDGETPL 74
Cdd:pfam13857   7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 24-77 8.66e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 54.29  E-value: 8.66e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 19076063   24 LDSGISPNAADENGYTPIHAAVSYGHSDLLKILVERGGDINIRDQDGETPLFVC 77
Cdd:PHA03100 179 LSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIA 232
Ank_4 pfam13637
Ankyrin repeats (many copies);
4-57 8.77e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.97  E-value: 8.77e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 19076063     4 TTPNIWIAASDGKTDVVLKHLDSGISPNAADENGYTPIHAAVSYGHSDLLKILV 57
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03095 PHA03095
ankyrin-like protein; Provisional
 17-121 9.04e-09

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 54.26  E-value: 9.04e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076063   17 TDVVLKHLDSGISPNAADENGYTPIHAAVSYGHS-DLLKILVERGGDINIRDQDGETPLFVCEK-LEIAHDLIN---QYN 91
Cdd:PHA03095  63 KDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTlDVIKLLIKAGADVNAKDKVGRTPLHVYLSgFNINPKVIRlllRKG 142

                         90       100       110
                 ....*....|....*....|....*....|.
gi 19076063   92 ADTTVKNNDGLIAAQV-IEANGEFPELAKYL 121
Cdd:PHA03095 143 ADVNALDLYGMTPLAVlLKSRNANVELLRLL 173
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 24-79 1.24e-07

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 51.05  E-value: 1.24e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 19076063   24 LDSGISPNAADENGYTPIHAAVSYGHSDLLKILVERGGDINIRDQDGETPLFVCEK 79
Cdd:PTZ00322 102 LTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEE 157
PHA03095 PHA03095
ankyrin-like protein; Provisional
 10-101 1.32e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 50.79  E-value: 1.32e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076063   10 IAASDGKTDVVLKHLDSGISPNAADENGYTPIHAAVSYGHSDLLKI---LVERGGDINIRDQDGETPLFVC----EKLEI 82
Cdd:PHA03095  20 LNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKDIvrlLLEAGADVNAPERCGFTPLHLYlynaTTLDV 99

                         90
                 ....*....|....*....
gi 19076063   83 AHDLInQYNADTTVKNNDG 101
Cdd:PHA03095 100 IKLLI-KAGADVNAKDKVG 117
Ank_4 pfam13637
Ankyrin repeats (many copies);
37-87 1.36e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.50  E-value: 1.36e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 19076063    37 GYTPIHAAVSYGHSDLLKILVERGGDINIRDQDGETPLFVC---EKLEIAHDLI 87
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAasnGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 7-75 2.68e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 50.25  E-value: 2.68e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19076063    7 NIWIAASDGKTDVVLKHLDSGISPNAADENGYTPIHAAVSYGHSDLLKILVERGGDINIRDQDGETPLF 75
Cdd:PLN03192 528 NLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALW 596
PHA03095 PHA03095
ankyrin-like protein; Provisional
 1-74 3.90e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 49.64  E-value: 3.90e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19076063    1 MSTTTPNIWIAA-SDGKTDVVLKHLDSGISPNAADENGYTPIHAAVSYGHSDLLKILVERGGDINIRDQDGETPL 74
Cdd:PHA03095 220 MLGNTPLHSMATgSSCKRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPL 294
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 36-65 1.35e-06

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 43.35  E-value: 1.35e-06
                           10        20        30
                   ....*....|....*....|....*....|
gi 19076063     36 NGYTPIHAAVSYGHSDLLKILVERGGDINI 65
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 8-101 1.37e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 47.74  E-value: 1.37e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076063    8 IWIAASDGKTDVVLKHLDSGISPNAADENGYTPIHAAVSYGHS-----DLLKILVERGGDINIRDQDGETPLFVC----- 77
Cdd:PHA03100  39 LYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAiskks 118

                         90       100
                 ....*....|....*....|....
gi 19076063   78 EKLEIAHDLINqYNADTTVKNNDG 101
Cdd:PHA03100 119 NSYSIVEYLLD-NGANVNIKNSDG 141
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 36-67 2.28e-06

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 42.66  E-value: 2.28e-06
                          10        20        30
                  ....*....|....*....|....*....|...
gi 19076063    36 NGYTPIHAAV-SYGHSDLLKILVERGGDINIRD 67
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 8-84 2.55e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 47.27  E-value: 2.55e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076063    8 IWIAASDGKTDVVLKHLDSGISPNAADENGYTPIHAAVSYGHSDLLKILVERGGDINIRDQDGETPL--------FVCEK 79
Cdd:PHA02874 128 LHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLhnaaeygdYACIK 207


                 ....*
gi 19076063   80 LEIAH 84
Cdd:PHA02874 208 LLIDH 212
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 11-102 6.82e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 46.03  E-value: 6.82e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076063   11 AASDGKTDVVLKHLDSGISPNAADENGYTPIHAAVSYGHS-DLLKILVERGGDINIRDQ-DGETPLFVCEKLEIAHDLIN 88
Cdd:PHA02878 208 AVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCKDyDILKLLLEHGVDVNAKSYiLGLTALHSSIKSERKLKLLL 287

                         90
                 ....*....|....
gi 19076063   89 QYNADTTVKNNDGL 102
Cdd:PHA02878 288 EYGADINSLNSYKL 301
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 36-65 7.38e-06

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 41.47  E-value: 7.38e-06
                          10        20        30
                  ....*....|....*....|....*....|
gi 19076063    36 NGYTPIHAAVSYGHSDLLKILVERGGDINI 65
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02798 PHA02798
ankyrin-like protein; Provisional
 14-107 1.40e-05

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 44.83  E-value: 1.40e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076063   14 DGKTDVVLKHLDSGISPNAADENGYTPIHAAVS----YGHS-DLLKILVERGGDINIRDQDGETPLF------VCEKLEI 82
Cdd:PHA02798  48 SPSTDIVKLFINLGANVNGLDNEYSTPLCTILSnikdYKHMlDIVKILIENGADINKKNSDGETPLYcllsngYINNLEI 127

                         90       100
                 ....*....|....*....|....*
gi 19076063   83 AHDLInQYNADTTVKNNDGLIAAQV 107
Cdd:PHA02798 128 LLFMI-ENGADTTLLDKDGFTMLQV 151
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 10-79 1.54e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 45.05  E-value: 1.54e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19076063   10 IAASDGKTDVVLkhLDSGISPNAADENGYTPIHAAV-SYGHSDLLKILVERGGDINIRDQDGETPLFVCEK 79
Cdd:PHA02876 248 IRNEDLETSLLL--YDAGFSVNSIDDCKNTPLHHASqAPSLSRLVPKLLERGADVNAKNIKGETPLYLMAK 316
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 29-101 3.53e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 43.80  E-value: 3.53e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19076063   29 SPNAADENGYTPIHAAVSYGHS-DLLKILVERGGDINIRDQDGETPLFVCEKLEIAHDLINQYNADTTVKNNDG 101
Cdd:PHA02874 246 SINDQDIDGSTPLHHAINPPCDiDIIDILLYHKADISIKDNKGENPIDTAFKYINKDPVIKDIIANAVLIKEAD 319
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 11-74 7.29e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 42.95  E-value: 7.29e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19076063   11 AASDGKTDVVLKHLDSGISPNAADENGYTPIHAAVSYGHSDLLKILVERGGDINIRDQDGETPL 74
Cdd:PHA02878 175 ATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPL 238
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 24-101 1.04e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 42.34  E-value: 1.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076063   24 LDSGISPNAADENGYTPIHAAVSYGHSDL--LKILVERGGDIN----------------IRDQDGETPLFVC---EKLEI 82
Cdd:PHA03100 128 LDNGANVNIKNSDGENLLHLYLESNKIDLkiLKLLIDKGVDINaknrvnyllsygvpinIKDVYGFTPLHYAvynNNPEF 207

                         90
                 ....*....|....*....
gi 19076063   83 AHDLINqYNADTTVKNNDG 101
Cdd:PHA03100 208 VKYLLD-LGANPNLVNKYG 225
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 11-74 1.45e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 41.90  E-value: 1.45e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19076063   11 AASDGKTDVVLKHLDSGISPNAADENGYTPIHAAVSYGHSDLLKILVERGGDINIRDQDGETPL 74
Cdd:PHA02875   9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESEL 72
PHA03095 PHA03095
ankyrin-like protein; Provisional
 16-74 2.22e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 41.16  E-value: 2.22e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19076063   16 KTDVVLKHLDSGISPNAADENGYTPIHAAVSYGHSDLLKI--LVERGGDINIRDQDGETPL 74
Cdd:PHA03095 201 RARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQTPL 261
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 24-74 5.24e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 40.43  E-value: 5.24e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 19076063   24 LDSGISPNAADENGYTPIHAAVSYGHSDLLKILVERGGDINIRDQDGETPL 74
Cdd:PHA02876 165 LEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVL 215
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 8-74 5.31e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 40.33  E-value: 5.31e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19076063    8 IWIAASDGKTDVVLKHLDSGISPNAADENGYTPIHAAVSYGHSDLLKILVERGGDINIRDQDGETPL 74
Cdd:PHA02874 161 IHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPL 227
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 18-101 5.76e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 39.95  E-value: 5.76e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076063   18 DVVLKHLDSGISPNAADENGYTPIHAAVSYGHSDLLKILVERGGDINIRDQDGETPLFVCEK---LEIAHDLINQyNADT 94
Cdd:PHA02874 105 DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKhnfFDIIKLLLEK-GAYA 183


                 ....*..
gi 19076063   95 TVKNNDG 101
Cdd:PHA02874 184 NVKDNNG 190
PHA02946 PHA02946
ankyin-like protein; Provisional
 24-75 9.39e-04

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 39.27  E-value: 9.39e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 19076063   24 LDSGISPNAADENGYTPIHAAVSYGHSDLLKILVERGGDINIRDQDGETPLF 75
Cdd:PHA02946  59 LHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLY 110
PHA03095 PHA03095
ankyrin-like protein; Provisional
 16-74 1.34e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 38.85  E-value: 1.34e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19076063   16 KTDVVLKHLDSGISPNAADENGYTPIHAAVSYGHSD--LLKILVERGGDINIRDQDGETPL 74
Cdd:PHA03095 131 NPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANveLLRLLIDAGADVYAVDDRFRSLL 191
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 44-102 1.92e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 38.46  E-value: 1.92e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19076063  44 AVSYGHSDLLKILVERGGDINIRDQDGETPL----------FVCEkleiAHDLINQYNAD------TTVKNNDGL 102
Cdd:cd22192 143 AACVGNEEIVRLLIEHGADIRAQDSLGNTVLhilvlqpnktFACQ----MYDLILSYDKEddlqplDLVPNNQGL 213
PHA02798 PHA02798
ankyrin-like protein; Provisional
 18-114 2.21e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 38.28  E-value: 2.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076063   18 DVVLKHLDSgispNAADENGYTPIHAAVSYGHSDLLKILVERGGDINIRDQDGETPLFVC---EKLEIAHDLINQYNADT 94
Cdd:PHA02798 243 DFIFSYIDI----NQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTAfenESKFIFNSILNKKPNKN 318

                         90       100
                 ....*....|....*....|
gi 19076063   95 TVKNNDGLIAAQVIEANGEF 114
Cdd:PHA02798 319 TISYTYYKLRKHILNVEGDF 338
PHA02917 PHA02917
ankyrin-like protein; Provisional
 31-72 3.33e-03

ankyrin-like protein; Provisional


Pssm-ID: 165231 [Multi-domain]  Cd Length: 661  Bit Score: 38.06  E-value: 3.33e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 19076063   31 NAADENGYTPIHAAVSYGHSDLLKILVERGGDINIRDQDGET 72
Cdd:PHA02917 446 NMIDKRGETLLHKAVRYNKQSLVSLLLESGSDVNIRSNNGYT 487
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 35-101 3.48e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 37.64  E-value: 3.48e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19076063   35 ENGYTPIHAAVSYGHSDLLKILVERggDINIRDQDGETPL-----FVCEKLEIahDLINQYNADTTVKNNDG 101
Cdd:PHA02874 221 KNGFTPLHNAIIHNRSAIELLINNA--SINDQDIDGSTPLhhainPPCDIDII--DILLYHKADISIKDNKG 288
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 10-112 6.59e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 37.15  E-value: 6.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076063   10 IAASDGKTDVVLKHLDSGISPNAADENGYTPIHAAVSYGHSDLLKILVE--------RGGDInirdqdgetplfVCE--- 78
Cdd:PLN03192 564 IAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHfasisdphAAGDL------------LCTaak 631

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 19076063   79 --KLEIAHDLINQ-YNADTtvKNNDGLIAAQVIEANG 112
Cdd:PLN03192 632 rnDLTAMKELLKQgLNVDS--EDHQGATALQVAMAED 666
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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